issue contents

Journal logoBIOLOGICAL
ISSN: 1399-0047

February 2008 issue

Highlighted illustration

Cover illustration: Active site of exonuclease I at 1.5 Å resolution with a TMP molecule bound. Omit electron density is contoured at 3[sigma]. Also observed is atypical coordination of two critical divalent cations which may be relevant to the mechanism of hydrolysis (p. 206).

research papers

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Surface-entropy reduction (SER) mutants of the FabF protein from S. pneumoniae were rationally designed to avoid the disruption of the presumably strong interfaces involved in the formation of a high-resolution (1.3 Å) crystal form while at the same time potentially destabilizing an undesirable crystal form. One of the mutant proteins yielded a new crystal form that diffracted to high resolution, underscoring the power of the SER approach in protein and crystal engineering.

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For the first time, protein microcrystallography has been performed with a focused synchrotron-radiation beam of 1 µm using a goniometer with a sub-micrometre sphere of confusion. The crystal structure of xylanase II has been determined with a flux density of about 3 × 1010 photons s−1 µm−2 at the sample.

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A novel methodological development for the analysis, via Raman microscopy, of SeMet-labelled protein crystals is presented.

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The computer program SnB, which implements the direct-methods Shake-and-Bake procedure and is part of the protein structure-determination package BnP, has recently been optimized in several ways for more rapid, automated substructure determination.

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Crystal structures of unliganded and liganded complexes of the A178L variant of dimeric and monomeric trypanosomal TIM are reported. The A178L point mutation changes the conserved sequence pattern of the C-terminal hinge of the catalytic loop-6. The point mutation causes differences in the apo structures but not in the liganded structures.

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Plastic microchannel crystallization template designs made from inexpensive cyclic olefin copolymers have been shown to be low-birefringent, X-ray transmissive and compatible with microfluidic fabrication in restricted geometry. The model proteins thaumatin, lysozyme and bacteriorhodopsin demonstrated the feasibility of conducting counter-diffusion equilibration within the new plastic configuration.

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The crystal structure of SCO0332 was determined; functional analysis suggests that SCO0332 is a transcriptional repressor of the sco0330 gene.

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The structure of Escherichia coli exonuclease I in complex with a nucleotide product, thymidine 5′-monophos­phate, is described in an orthorhombic space group at 1.5 Å resolution.

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The crystal structure of methionine γ-lyase from Citrobacter freundii was determined at 1.35 Å. The high-resolution structure makes it possible to analyze in detail interactions between monomers, a mode of the cofactor binding and participation of the protein flexible regions in substrate recognition and binding.

short communications

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The noncrystallographic symmetry operations reported for two crystal structures of 3,4-dihydroxy-2-butanone 4-phosphate synthase can be reinterpreted as crystallographic operations.

international union of crystallography

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